Inside Cover: Enantioselective Reduction of Citral Isomers in NCR Ene Reductase: Analysis of an Active‐Site Mutant Library (ChemBioChem 8/2017)

The inside cover picture shows the ene reductase NCR as a “lemon press” converting either the (E)‐ or the (Z)‐citral isomer to citronellal juice. Tryptophan residue 66 (marked in orange) or the alanine counterpart (red) at this position decides whether the juice contains (S)‐ or (R)‐citronellal. The...

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Bibliographic Details
Published in:Chembiochem : a European journal of chemical biology 2017-04, Vol.18 (8), p.695-695
Main Authors: Kress, Nico, Rapp, Johanna, Hauer, Bernhard
Format: Article
Language:English
Subjects:
citral reduction
isomers
NCR ene reductase
protein engineering
structure-activity relationships
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Summary:The inside cover picture shows the ene reductase NCR as a “lemon press” converting either the (E)‐ or the (Z)‐citral isomer to citronellal juice. Tryptophan residue 66 (marked in orange) or the alanine counterpart (red) at this position decides whether the juice contains (S)‐ or (R)‐citronellal. The development of an R‐selective citral reduction catalyst is of industrial importance for the synthesis of aroma chemicals such as (−)‐menthol. The active‐site‐mutagenesis study presented in this paper reveals an important discrimination of the citral isomers by NCR ene reductase More information can be found in the communication by B. Hauer et al. on page 717 in Issue 8, 2017 (DOI: 10.1002/cbic.201700011).
ISSN:1439-4227
1439-7633
DOI:10.1002/cbic.201700163